ArticleMethodsX2014
Comparative analysis and validation of the malachite green assay for the high throughput biochemical characterization of terpene synthases.
Article in MethodsX, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 54 citations in OpenAlex.
- Review
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- Structural basis for the catalytic mechanism of human lipid phosphate phosphatases.Nature chemical biology · 2026Article
- A tailored CoA ligase-Nature catalysis · 2026Article
- Optimization of a malachite green-pyrophosphatase assay for the Zika virus RNA-dependent RNA polymerase and preliminary identification of natural product modulators.Frontiers in drug discovery · 2026Article
- Characterization of the Cubamyces Menziesii Terpenome.Chembiochem : a European journal of chemical biology · 2025Article
- Discovery of Inhibitors Targeting the RNA-Dependent RNA Polymerase of the Zika Virus.bioRxiv : the preprint server for biology · 2025Article
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- Structural insights into human ABCD3-mediated peroxisomal acyl-CoA translocation.Cell discovery · 2024Article
- Transport mechanism of human bilirubin transporter ABCC2 tuned by the inter-module regulatory domain.Nature communications · 2024Article
- Decoding Catalysis by Terpene Synthases.ACS catalysis · 2023Review
- Metabolite interactions in the bacterial Calvin cycle and implications for flux regulation.Communications biology · 2023Article
- Placing steroid hormones within the human ABCC3 transporter reveals a compatible amphiphilic substrate-binding pocket.The EMBO journal · 2023Article
- The Bacteriophage-Phage-Inducible Chromosomal Island Arms Race Designs an Interkingdom Inhibitor of dUTPases.Microbiology spectrum · 2023Article
- Predictive Engineering of Class I Terpene Synthases Using Experimental and Computational Approaches.Chembiochem : a European journal of chemical biology · 2022Review
- Synthetic biology, combinatorial biosynthesis, and chemo‑enzymatic synthesis of isoprenoids.Journal of industrial microbiology & biotechnology · 2020Review
- Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Terpenes are the largest group of natural products with important and diverse biological roles, while of tremendous economic value as fragrances, flavours and pharmaceutical agents. Class-I terpene synthases (TPSs), the dominant type of TPS enzymes, catalyze the conversion of prenyl diphosphates to often structurally diverse bioactive terpene hydrocarbons, and inorganic pyrophosphate (PPi). To measure their kinetic properties, current bio-analytical methods typically rely on the direct detection of hydrocarbon products by radioactivity measurements or gas chromatography-mass spectrometry (GC-MS). In this study we employed an established, rapid colorimetric assay, the pyrophosphate/malachite green assay (MG), as an alternative means for the biochemical characterization of class I TPSs activity.•We describe the adaptation of the MG assay for turnover and catalytic efficiency measurements of TPSs.•We validate the method by direct comparison with established assays. The agreement of k cat/K M among methods makes this adaptation optimal for rapid evaluation of TPSs.•We demonstrate the application of the MG assay for the high-throughput screening of TPS gene libraries.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.